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In this study, we describe the characterization of a new lectin, BfL-II, purified from the seeds of Bauhinia forficata, which is distinct, at sequence-level, from the previously reported lectin from the same specie (BfL). In addition, the gene for this lectin was cloned and expressed in Escherichia coli and its antiproliferative activity was evaluated against human breast and colorectal cancer cells (MCF-7 and HT-29, respectively). The treatment with 100 μg/μL of either native or recombinant BfL (nBfL or rBfL) significantly reduced the proliferation of both cancer cell lines (p < 0.01). The inhibition of HT-29 cell proliferation was as high as 82.5% and 93.6% with 100 μg/μL of rBfL-I and nBfL after 24 h, respectively. Therefore, BfL-II presents a promising antiproliferative activity, which may be applied in the development of new anticancer treatments.
This article was published in the following journal.
Name: International journal of biological macromolecules
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A specific mannose-binding member of the collectin family of lectins. It binds to carbohydrate groups on invading pathogens and plays a key role in the MANNOSE-BINDING LECTIN COMPLEMENT PATHWAY.
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Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.
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Track and monitor developments in breast cancer research and commercial development. Follow the tabs above to read the latest global news, research, clinical trials on breast cancer and follow companies active in the development of breast cancer tr...